Post-translational modifications of RGS protein family: Pivotal switches in cellular signaling transduction and diseases
Regulator of G protein signaling (RGS) proteins are critical modulators of G protein-coupled receptor (GPCR) signaling through their GTPase-activating protein (GAP) activity. RGS proteins are regulated at multiple levels, including the pre-transcription, transcription, and post-translation levels. A...
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| Format: | Article |
| Language: | English |
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Elsevier
2025-07-01
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| Series: | Pharmacological Research |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S1043661825002269 |
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| author | Yan Song Zihao An Jiepu Wang Qiang Xu Jiayong Li Chao Tang |
| author_facet | Yan Song Zihao An Jiepu Wang Qiang Xu Jiayong Li Chao Tang |
| author_sort | Yan Song |
| collection | DOAJ |
| description | Regulator of G protein signaling (RGS) proteins are critical modulators of G protein-coupled receptor (GPCR) signaling through their GTPase-activating protein (GAP) activity. RGS proteins are regulated at multiple levels, including the pre-transcription, transcription, and post-translation levels. Among the regulation patterns, post-translational modification (PTMs) can directly affect the regulation of G protein signaling by modulating the GAP activity of RGS proteins or indirectly regulate their function by affecting their subcellular localization and stability. The corresponding PTM behavior of a certain RGS protein is regulated by complex upstream factors and is closely related to multiple downstream signal transduction associated with G proteins. This complex regulatory relationship forms a dynamic and fine-tuned regulatory network within the cell. In this review, we methodically summarize the impact of diverse PTMs on RGS proteins and provide a comprehensive overview of their associated upstream regulatory factors and downstream signal pathway alterations. Furthermore, we explore the physiological and pathological states associated with PTM dysregulation. Additionally, we discuss the potential clinical application value of PTMs targeting RGS. |
| format | Article |
| id | doaj-art-c1180ebf685b4488860d570fe13d99bc |
| institution | OA Journals |
| issn | 1096-1186 |
| language | English |
| publishDate | 2025-07-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Pharmacological Research |
| spelling | doaj-art-c1180ebf685b4488860d570fe13d99bc2025-08-20T02:34:35ZengElsevierPharmacological Research1096-11862025-07-0121710780110.1016/j.phrs.2025.107801Post-translational modifications of RGS protein family: Pivotal switches in cellular signaling transduction and diseasesYan Song0Zihao An1Jiepu Wang2Qiang Xu3Jiayong Li4Chao Tang5National Clinical Research Center for Child Health of Children's Hospital, Zhejiang University School of Medicine, Hangzhou 310052, ChinaNational Clinical Research Center for Child Health of Children's Hospital, Zhejiang University School of Medicine, Hangzhou 310052, ChinaNational Clinical Research Center for Child Health of Children's Hospital, Zhejiang University School of Medicine, Hangzhou 310052, ChinaNational Clinical Research Center for Child Health of Children's Hospital, Zhejiang University School of Medicine, Hangzhou 310052, ChinaState Key Laboratory of Ophthalmology, Zhongshan Ophthalmic Center, Sun Yat-sen University, Guangzhou 510060, ChinaNational Clinical Research Center for Child Health of Children's Hospital, Zhejiang University School of Medicine, Hangzhou 310052, China; Corresponding author.Regulator of G protein signaling (RGS) proteins are critical modulators of G protein-coupled receptor (GPCR) signaling through their GTPase-activating protein (GAP) activity. RGS proteins are regulated at multiple levels, including the pre-transcription, transcription, and post-translation levels. Among the regulation patterns, post-translational modification (PTMs) can directly affect the regulation of G protein signaling by modulating the GAP activity of RGS proteins or indirectly regulate their function by affecting their subcellular localization and stability. The corresponding PTM behavior of a certain RGS protein is regulated by complex upstream factors and is closely related to multiple downstream signal transduction associated with G proteins. This complex regulatory relationship forms a dynamic and fine-tuned regulatory network within the cell. In this review, we methodically summarize the impact of diverse PTMs on RGS proteins and provide a comprehensive overview of their associated upstream regulatory factors and downstream signal pathway alterations. Furthermore, we explore the physiological and pathological states associated with PTM dysregulation. Additionally, we discuss the potential clinical application value of PTMs targeting RGS.http://www.sciencedirect.com/science/article/pii/S1043661825002269RGSPTMsCell signalingDisease mechanismClinical application |
| spellingShingle | Yan Song Zihao An Jiepu Wang Qiang Xu Jiayong Li Chao Tang Post-translational modifications of RGS protein family: Pivotal switches in cellular signaling transduction and diseases Pharmacological Research RGS PTMs Cell signaling Disease mechanism Clinical application |
| title | Post-translational modifications of RGS protein family: Pivotal switches in cellular signaling transduction and diseases |
| title_full | Post-translational modifications of RGS protein family: Pivotal switches in cellular signaling transduction and diseases |
| title_fullStr | Post-translational modifications of RGS protein family: Pivotal switches in cellular signaling transduction and diseases |
| title_full_unstemmed | Post-translational modifications of RGS protein family: Pivotal switches in cellular signaling transduction and diseases |
| title_short | Post-translational modifications of RGS protein family: Pivotal switches in cellular signaling transduction and diseases |
| title_sort | post translational modifications of rgs protein family pivotal switches in cellular signaling transduction and diseases |
| topic | RGS PTMs Cell signaling Disease mechanism Clinical application |
| url | http://www.sciencedirect.com/science/article/pii/S1043661825002269 |
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